Collagen is the body's major structural protein. It is composed of three protein chains wound together in a tight triple helix to form fibrils. The fibrils are cross-linked in the extracellular matrix to provide the structural scaffolding surrounding cells that helps to support cell shape and differentiation. The mesh-like collagen network binds cells together and provides the supportive framework or environment in which cells develop and function. The stimulation of collagen gives the skin its strength, durability, and smooth, plump appearance.
N-Acetyl-Tyrosinamide is an amino acid derivative with potent anti-aging and cosmetic benefits, as described in U.S. Pat. No. RE 41,278 and U.S. Pat. No. RE 41,339, the disclosures of which are hereby incorporated by reference. The present inventors have investigated the mode of operation of N-Acetyl-Tyrosinamide and discovered that it is a potent stimulator of the enzyme PLOD-2 (procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2 (lysine hydroxylase-2), a homodimeric enzyme that is critical in the collagen maturation process.
Collagen synthesis and maturation is a complex multistep process. The PLOD-2 enzyme plays a fundamental role in the collagen maturation process; it catalyzes the hydroxylation of lysine residues in the nascent procollagen protein strands. The resultant hydroxylysyl groups aid in the formation of the triple helix and serve as attachment sites for cross linking in the extracellular matrix. See, Van der Slot et al., 2003, J. Biol. Chem., 278:40967-40972; Walker et al., 2005, Matrix Biology, 23:515-523; Wu et al., 2006, Exp. Cell Res., 312:3485-3494. Thus, this modification is critical for the stability of procollagen, the intermolecular cross linking of collagen fibrils and ultimately the maintenance of the dermal matrix.
The foregoing discussion is presented solely to provide a better understanding of the nature of the problems confronting the art and should not be construed in any way as an admission as to prior art.